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Updated: Jun 9, 2026

Imaging InlC Secretion to Investigate Cellular Infection by the Bacterial Pathogen Listeria monocytogenes
Published on: September 19, 2013
Listeria monocytogenes PrsA2 is required for virulence factor secretion and bacterial viability within the host cell
Francis Alonzo1, Nancy E Freitag
1Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, IL 60612-7344, USA.
Abstract:
In the course of establishing its replication niche within the cytosol of infected host cells, the facultative intracellular bacterial pathogen Listeria monocytogenes must efficiently regulate the secretion and activity of multiple virulence factors. L. monocytogenes encodes two predicted posttranslocation secretion chaperones, PrsA1 and PrsA2, and evidence suggests that PrsA2 has been specifically adapted for bacterial pathogenesis. PrsA-like chaperones have been identified in a number of Gram-positive bacteria, where they are reported to function at the bacterial membrane-cell wall interface to assist in the folding of proteins translocated across the membrane; in some cases, these proteins have been found to be essential for bacterial viability. In this study, the contributions of PrsA2 and PrsA1 to L. monocytogenes growth and protein secretion were investigated in vitro and in vivo. Neither PrsA2 nor PrsA1 was found to be essential for L. monocytogenes growth in broth culture; however, optimal bacterial viability was found to be dependent upon PrsA2 for L. monocytogenes located within the cytosol of host cells. Proteomic analyses of prsA2 mutant strains in the presence of a mutationally activated allele of the virulence regulator PrfA revealed a critical requirement for PrsA2 activity under conditions of PrfA activation, an event which normally takes place within the host cell cytosol. Despite a high degree of amino acid similarity, no detectable degree of functional overlap was observed between PrsA2 and PrsA1. Our results indicate a critical requirement for PrsA2 under conditions relevant to host cell infection.
Insights
The bacterial chaperone PrsA2 is crucial for Listeria monocytogenes survival within host cells, aiding virulence factor secretion. PrsA1 does not provide functional overlap, highlighting PrsA2's specific role in pathogenesis.
Area of Science:
- Microbiology
- Bacterial Pathogenesis
- Host-Pathogen Interactions
Background:
- Facultative intracellular bacteria like Listeria monocytogenes require precise regulation of virulence factors for host cell invasion.
- Post-translocation secretion chaperones, such as PrsA1 and PrsA2 in L. monocytogenes, are implicated in protein folding and secretion at the bacterial membrane-cell wall interface.
- PrsA2 is suggested to be specifically adapted for bacterial pathogenesis.
Purpose of the Study:
- To investigate the roles of PrsA1 and PrsA2 in Listeria monocytogenes growth and protein secretion.
- To determine the necessity of PrsA2 for bacterial viability within host cell cytosol.
- To elucidate the functional relationship between PrsA1 and PrsA2.
Main Methods:
- In vitro and in vivo growth assays for L. monocytogenes strains lacking PrsA1 or PrsA2.
- Proteomic analysis of prsA2 mutant strains under conditions of activated virulence regulator PrfA.
- Comparison of amino acid sequences and functional overlap between PrsA1 and PrsA2.
Main Results:
- Neither PrsA1 nor PrsA2 was essential for L. monocytogenes growth in broth culture.
- Optimal bacterial viability within host cell cytosol was dependent on PrsA2.
- PrsA2 activity was critically required under conditions of PrfA activation, mimicking host cell infection.
- No functional overlap was detected between PrsA2 and PrsA1 despite high sequence similarity.
Conclusions:
- PrsA2 plays a critical role in Listeria monocytogenes pathogenesis, particularly within the host cell cytosol.
- PrsA2 is essential for bacterial viability and virulence factor regulation during host cell infection.
- PrsA1 and PrsA2 are functionally distinct, with PrsA2 uniquely adapted for infection-related processes.
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